In silico approach for designing potent inhibitors against tyrosinase

Abstract

In recent years regulation of the enzymatic activity of tyrosinase has been the main focus of investigation due to its potential applications in medicine, agriculture and cosmetics. In the present study, Eighteen derivatives of 3-hydroxypyridine-4-one scaffold were subjected to molecular docking studies to investigating the mode of interaction of the compounds with tyrosinase active site. We applied Autodock tools 4.2, in order to set up the docking runs and predict the inhibitors binding free energy. The final product of molecular docking was clustered to specify the binding free energy and optimal docking energy conformation that is investigated as the best docked structure. Among the total of molecules tested, it was proved that Ligands 3, and 10 have the lowest binding free energy. The docked conformation revealed that these compounds could form metal-ligand interaction with The Cu2+ ions in the active site. These insilico results can thus serve as a template for further studies invitro and invivo.